Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
119000 | - |
- |
Paracoccus denitrificans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Paracoccus denitrificans | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | the diheme enzymeMauG catalyzes the post-translational modification of a precursor protein of methylamine dehydrogenase, preMADH, to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone, TTQ, cofactor. This six-electron oxidation of preMADH requires long-range electron transfer as the structure of the MauG-preMADH complex reveals that the shortest distance between the modified residues of preMADH and the nearest heme of MauG is 14.0 A. Steady-state kinetic and single turnover kinetic studies of MauG-dependent oxidation of quinol MADH at pH 7.5, 25°C, overview | Paracoccus denitrificans |
Subunits | Comment | Organism |
---|---|---|
heterotetramer | alpha2beta2 protein, with each beta subunit possessing a tryptophan tryptophylquinone, TTQ, protein-derived cofactor | Paracoccus denitrificans |
Synonyms | Comment | Organism |
---|---|---|
MADH | - |
Paracoccus denitrificans |
methylamine dehydrogenase | - |
Paracoccus denitrificans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
tryptophan tryptophylquinone | a two-electron redox cofactor, each beta subunit of the heterotetrameric enzyme NADH possesses a tryptophan tryptophylquinone, TTQ, protein-derived cofactor. TTQ is formed by post-translational modification of two tryptophan residues of the preMADH polypeptide chain through the diheme enzyme MauG. This six-electron oxidation of preMADH requires long-range electron transfer as the structure of the MauG-preMADH complex reveals that the shortest distance between the modified residues of preMADH and the nearest heme of MauG is 14.0 A, overview | Paracoccus denitrificans |
General Information | Comment | Organism |
---|---|---|
additional information | steady-state MauG-depedent TTQ biosynthesis using quinol MADH as a substrate and single-turnover kinetics of the reaction of bis-Fe(IV) MauG with quinol MADH, overview | Paracoccus denitrificans |